Reviewed,
UniProtKB/Swiss-Prot Q63716 (PRDX1_RAT)
Last modified
November 25, 2008.
Version 79.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Peroxiredoxin-1 EC=1.11.1.15 Alternative name(s): Thioredoxin peroxidase 2 Thioredoxin-dependent peroxide reductase 2 Heme-binding 23 kDa protein HBP23 | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 199 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). |
| Catalytic activity | 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. |
| Subunit structure | Homodimer; disulfide-linked, upon oxidation. May form heterodimers with AOP2. |
| Subcellular location | Cytoplasm. MelanosomeBy similarity. |
| Post-translational modification | Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity By similarity. |
| Miscellaneous | The active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin. Inactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be irreversibly oxidized. |
| Sequence similarities | Belongs to the ahpC/TSA family. Contains 1 thioredoxin domain. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Domain | Redox-active center |
| Molecular function | Antioxidant Oxidoreductase Peroxidase |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | peroxiredoxin activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 199 | 199 | Peroxiredoxin-1 | PRO_0000135078 | |||||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||||
| Domain | 6 – 165 | 160 | Thioredoxin | ||||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||||
| Active site | 52 | 1 | Cysteine sulfenic acid (-SOH) intermediate | ||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 90 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 183 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 194 | 1 | Phosphotyrosine By similarity | ||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 52 | Interchain (with C-173); in linked form | |||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 173 | Interchain (with C-52); in linked form | |||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 16 – 20 | 5 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 26 – 30 | 5 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 31 – 34 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 37 – 43 | 7 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 50 – 52 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 57 – 61 | 5 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 63 – 68 | 6 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 71 – 78 | 8 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 81 – 88 | 8 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 92 – 94 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 104 – 106 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 111 – 115 | 5 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 121 – 124 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 128 – 133 | 6 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 137 – 145 | 9 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 153 – 168 | 16 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 170 – 172 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Turn | 188 – 191 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 192 – 195 | 4 | |||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Purification, characterization, and cloning of a heme-binding protein (23 kDa) in rat liver cytosol." Iwahara S., Satoh H., Song D.-X., Webb J., Burlingame A.L., Nagae Y., Mueller-Eberhard U. Biochemistry 34:13398-13406(1995) [PubMed: 7577926] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver and Pituitary. |
| [3] | Lubec G., Afjehi-Sadat L., Diao W., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 17-35 AND 111-190, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain, Hippocampus and Spinal cord. |
| [4] | "Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product." Hirotsu S., Abe Y., Okada K., Nagahara N., Hori H., Nishino T., Hakoshima T. Proc. Natl. Acad. Sci. U.S.A. 96:12333-12338(1999) [PubMed: 10535922] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN OXIDIZED FORM. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| D30035 mRNA. Translation: BAA06275.1. BC058450 mRNA. Translation: AAH58450.1. BC088118 mRNA. Translation: AAH88118.1. | |||||||||||||||||||
| PIR | I52425. | ||||||||||||||||||
| RefSeq | NP_476455.1. | ||||||||||||||||||
| UniGene | Rn.2845 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||
Protein family/group databases | |||||||||||||||||||
| PeroxiBase | 4508. Rno2CysPrx01. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | Q63716. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENSRNOG00000017194. Rattus norvegicus. [Contig view] | ||||||||||||||||||
| GeneID | 117254. | ||||||||||||||||||
| KEGG | rno:117254. | ||||||||||||||||||
| NMPDR | fig|10116.3.peg.23718. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| RGD | 620039. Prdx1. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOVERGEN | Q63716. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| GermOnline | ENSRNOG00000017194. Rattus norvegicus. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR000866. AhpC-TSA. IPR012335. Thioredoxin_fold. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. | ||||||||||||||||||
| Pfam | PF00578. AhpC-TSA. 1 hit. [Graphical view] | ||||||||||||||||||
| PROSITE | PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| NextBio | 620108. | ||||||||||||||||||
Entry information
| Entry name | PRDX1_RAT | ||||||||
| Accession | Primary (citable) accession number: Q63716 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


